ArticleFrontiers in bioengineering and biotechnology2014
The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence.
Article in Frontiers in bioengineering and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Elastin-like polypeptide and γ-zein fusions significantly increase recombinant protein accumulation in soybean seeds.Transgenic research · 2021Article
- Characterization and Immunogenicity of HIV Envelope gp140 ZeraFrontiers in bioengineering and biotechnology · 2020Article
- 3D Electron Microscopy Gives a Clue: Maize Zein Bodies Bud From Central Areas of ER Sheets.Frontiers in plant science · 2020Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
- LALFPlant biotechnology journal · 2018Article
- Protein bodies: how the ER deals with high accumulation of recombinant proteins.Plant biotechnology journal · 2017Article
- High CO2 concentration as an inductor agent to drive production of recombinant phytotoxic antimicrobial peptides in plant biofactories.Plant molecular biology · 2016Article
- The Encapsulation of Hemagglutinin in Protein Bodies Achieves a Stronger Immune Response in Mice than the Soluble Antigen.Frontiers in plant science · 2016Article
- Application of a Scalable Plant Transient Gene Expression Platform for Malaria Vaccine Development.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
Naturally occurring storage proteins such as zeins are used as fusion partners for recombinant proteins because they induce the formation of ectopic storage organelles known as protein bodies (PBs) where the proteins are stabilized by intermolecular interactions and the formation of disulfide bonds. Endogenous PBs are derived from the endoplasmic reticulum (ER). Here, we have used different targeting sequences to determine whether ectopic PBs composed of the N-terminal portion of mature 27 kDa γ-zein added to a fluorescent protein could be induced to form elsewhere in the cell. The addition of a transit peptide for targeting to plastids causes PB formation in the stroma, whereas in the absence of any added targeting sequence PBs were typically associated with the plastid envelope, revealing the presence of a cryptic plastid-targeting signal within the γ-zein cysteine-rich domain. The subcellular localization of the PBs influences their morphology and the solubility of the stored recombinant fusion protein. Our results indicate that the biogenesis and budding of PBs does not require ER-specific factors and therefore, confirm that γ-zein is a versatile fusion partner for recombinant proteins offering unique opportunities for the accumulation and bioencapsulation of recombinant proteins in different subcellular compartments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.